ID DER_BACSU Reviewed; 436 AA. AC P50743; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 27-MAR-2024, entry version 158. DE RecName: Full=GTPase Der; DE AltName: Full=GTP-binding protein EngA; GN Name=der; Synonyms=engA, yphC; OrderedLocusNames=BSU22840; OS Bacillus subtilis (strain 168). OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=224308; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / RC NCIMB 3610 / NRRL NRS-744 / VKM B-501; RX PubMed=8760912; DOI=10.1099/13500872-142-8-2005; RA Sorokin A.V., Azevedo V., Zumstein E., Galleron N., Ehrlich S.D., RA Serror P.; RT "Sequence analysis of the Bacillus subtilis chromosome region between the RT serA and kdg loci cloned in a yeast artificial chromosome."; RL Microbiology 142:2005-2016(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=168; RX PubMed=9384377; DOI=10.1038/36786; RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K., RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., RA Yoshikawa H., Danchin A.; RT "The complete genome sequence of the Gram-positive bacterium Bacillus RT subtilis."; RL Nature 390:249-256(1997). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 185-436. RC STRAIN=168; RX PubMed=7592341; DOI=10.1128/jb.177.20.5899-5905.1995; RA Morbidoni H.R., de Mendoza D., Cronan J.E. Jr.; RT "Synthesis of sn-glycerol 3-phosphate, a key precursor of membrane lipids, RT in Bacillus subtilis."; RL J. Bacteriol. 177:5899-5905(1995). RN [4] RP GTP- AND GDP-BINDING, PROTEIN LEVELS, AND DISRUPTION PHENOTYPE. RC STRAIN=CRK6000; RX PubMed=12427945; DOI=10.1099/00221287-148-11-3539; RA Morimoto T., Loh P.C., Hirai T., Asai K., Kobayashi K., Moriya S., RA Ogasawara N.; RT "Six GTP-binding proteins of the Era/Obg family are essential for cell RT growth in Bacillus subtilis."; RL Microbiology 148:3539-3552(2002). RN [5] RP INTERACTION WITH THE 50S RIBOSOMAL SUBUNIT, AND FUNCTION IN 50S RIBOSOMAL RP SUBUNIT BIOGENESIS. RC STRAIN=RB247; RX PubMed=16997968; DOI=10.1128/jb.01213-06; RA Schaefer L., Uicker W.C., Wicker-Planquart C., Foucher A.-E., Jault J.-M., RA Britton R.A.; RT "Multiple GTPases participate in the assembly of the large ribosomal RT subunit in Bacillus subtilis."; RL J. Bacteriol. 188:8252-8258(2006). RN [6] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) BOUND TO GDP IN THE PROBABLE OFF RP STATE. RX PubMed=16894162; DOI=10.1073/pnas.0602585103; RA Muench S.P., Xu L., Sedelnikova S.E., Rice D.W.; RT "The essential GTPase YphC displays a major domain rearrangement associated RT with nucleotide binding."; RL Proc. Natl. Acad. Sci. U.S.A. 103:12359-12364(2006). CC -!- FUNCTION: GTPase that plays an essential role in the late steps of CC ribosome biogenesis. {ECO:0000269|PubMed:16997968}. CC -!- SUBUNIT: Cofractionates with the 70S ribosome; association is CC stabilized by the non-hydrolyzable GTP analog GMPPNP, and inhibited by CC GTP or GDP. CC -!- DISRUPTION PHENOTYPE: Essential for growth, it cannot be disrupted. CC Depletion experiments show that cells become longer and abnormally CC curved, with nucleoid condensation. Cells have many fewer 70S CC ribosomes; the large ribosomal subunit is 45S and is missing proteins CC L16, L27, L36 and interacts with 2 large non-ribosomal proteins. CC {ECO:0000269|PubMed:12427945}. CC -!- MISCELLANEOUS: Estimated to be present at 7000 copies per cell. CC -!- SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like CC GTPase superfamily. EngA (Der) GTPase family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=U32164; Type=Frameshift; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; L47648; AAC83966.1; -; Genomic_DNA. DR EMBL; AL009126; CAB14200.1; -; Genomic_DNA. DR EMBL; U32164; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR PIR; A69936; A69936. DR RefSeq; NP_390165.1; NC_000964.3. DR RefSeq; WP_003230565.1; NZ_JNCM01000036.1. DR PDB; 2HJG; X-ray; 2.50 A; A=1-436. DR PDB; 4DCS; X-ray; 2.25 A; A=1-436. DR PDB; 4DCT; X-ray; 2.30 A; A=1-436. DR PDB; 4DCU; X-ray; 2.00 A; A=1-436. DR PDB; 4DCV; X-ray; 2.60 A; A=1-436. DR PDB; 5M7H; X-ray; 3.15 A; A=1-436. DR PDB; 5MBS; X-ray; 3.20 A; A=1-436. DR PDB; 5X4B; X-ray; 1.50 A; A/B=2-163. DR PDBsum; 2HJG; -. DR PDBsum; 4DCS; -. DR PDBsum; 4DCT; -. DR PDBsum; 4DCU; -. DR PDBsum; 4DCV; -. DR PDBsum; 5M7H; -. DR PDBsum; 5MBS; -. DR PDBsum; 5X4B; -. DR AlphaFoldDB; P50743; -. DR SMR; P50743; -. DR STRING; 224308.BSU22840; -. DR jPOST; P50743; -. DR PaxDb; 224308-BSU22840; -. DR EnsemblBacteria; CAB14200; CAB14200; BSU_22840. DR GeneID; 938988; -. DR KEGG; bsu:BSU22840; -. DR PATRIC; fig|224308.179.peg.2489; -. DR eggNOG; COG1160; Bacteria. DR InParanoid; P50743; -. DR OrthoDB; 9805918at2; -. DR PhylomeDB; P50743; -. DR BioCyc; BSUB:BSU22840-MONOMER; -. DR EvolutionaryTrace; P50743; -. DR Proteomes; UP000001570; Chromosome. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule. DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central. DR GO; GO:0042254; P:ribosome biogenesis; IEA:UniProtKB-KW. DR CDD; cd01894; EngA1; 1. DR CDD; cd01895; EngA2; 1. DR Gene3D; 3.30.300.20; -; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2. DR HAMAP; MF_00195; GTPase_Der; 1. DR InterPro; IPR031166; G_ENGA. DR InterPro; IPR006073; GTP-bd. DR InterPro; IPR016484; GTPase_Der. DR InterPro; IPR032859; KH_dom-like. DR InterPro; IPR015946; KH_dom-like_a/b. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR NCBIfam; TIGR03594; GTPase_EngA; 1. DR NCBIfam; TIGR00231; small_GTP; 2. DR PANTHER; PTHR43834; GTPASE DER; 1. DR PANTHER; PTHR43834:SF6; GTPASE DER; 1. DR Pfam; PF14714; KH_dom-like; 1. DR Pfam; PF01926; MMR_HSR1; 2. DR PIRSF; PIRSF006485; GTP-binding_EngA; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2. DR PROSITE; PS51712; G_ENGA; 2. PE 1: Evidence at protein level; KW 3D-structure; GTP-binding; Nucleotide-binding; Reference proteome; Repeat; KW Ribosome biogenesis. FT CHAIN 1..436 FT /note="GTPase Der" FT /id="PRO_0000178964" FT DOMAIN 4..167 FT /note="EngA-type G 1" FT DOMAIN 176..351 FT /note="EngA-type G 2" FT DOMAIN 352..436 FT /note="KH-like" FT BINDING 10..17 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /ligand_label="1" FT /evidence="ECO:0000255" FT BINDING 57..61 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /ligand_label="1" FT /evidence="ECO:0000255" FT BINDING 119..122 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /ligand_label="1" FT /evidence="ECO:0000255" FT BINDING 182..189 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /ligand_label="2" FT /evidence="ECO:0000255" FT BINDING 229..233 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /ligand_label="2" FT /evidence="ECO:0000255" FT BINDING 294..297 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /ligand_label="2" FT /evidence="ECO:0000255" FT CONFLICT 186..187 FT /note="VG -> CR (in Ref. 2)" FT /evidence="ECO:0000305" FT STRAND 4..9 FT /evidence="ECO:0007829|PDB:5X4B" FT STRAND 12..15 FT /evidence="ECO:0007829|PDB:5X4B" FT HELIX 16..23 FT /evidence="ECO:0007829|PDB:5X4B" FT STRAND 24..28 FT /evidence="ECO:0007829|PDB:4DCU" FT STRAND 30..32 FT /evidence="ECO:0007829|PDB:5MBS" FT STRAND 42..48 FT /evidence="ECO:0007829|PDB:5X4B" FT STRAND 51..57 FT /evidence="ECO:0007829|PDB:5X4B" FT HELIX 58..60 FT /evidence="ECO:0007829|PDB:5X4B" FT HELIX 68..82 FT /evidence="ECO:0007829|PDB:5X4B" FT STRAND 84..91 FT /evidence="ECO:0007829|PDB:5X4B" FT TURN 92..94 FT /evidence="ECO:0007829|PDB:5X4B" FT HELIX 98..107 FT /evidence="ECO:0007829|PDB:5X4B" FT STRAND 114..119 FT /evidence="ECO:0007829|PDB:5X4B" FT HELIX 124..136 FT /evidence="ECO:0007829|PDB:5X4B" FT STRAND 137..139 FT /evidence="ECO:0007829|PDB:5X4B" FT STRAND 141..143 FT /evidence="ECO:0007829|PDB:5X4B" FT TURN 146..149 FT /evidence="ECO:0007829|PDB:5X4B" FT HELIX 152..161 FT /evidence="ECO:0007829|PDB:5X4B" FT HELIX 162..165 FT /evidence="ECO:0007829|PDB:2HJG" FT STRAND 176..181 FT /evidence="ECO:0007829|PDB:4DCU" FT STRAND 183..187 FT /evidence="ECO:0007829|PDB:5M7H" FT HELIX 188..196 FT /evidence="ECO:0007829|PDB:4DCU" FT STRAND 201..203 FT /evidence="ECO:0007829|PDB:4DCU" FT STRAND 215..220 FT /evidence="ECO:0007829|PDB:4DCU" FT STRAND 223..227 FT /evidence="ECO:0007829|PDB:4DCU" FT HELIX 230..232 FT /evidence="ECO:0007829|PDB:4DCU" FT TURN 233..235 FT /evidence="ECO:0007829|PDB:4DCU" FT TURN 236..238 FT /evidence="ECO:0007829|PDB:4DCT" FT HELIX 245..257 FT /evidence="ECO:0007829|PDB:4DCU" FT STRAND 259..266 FT /evidence="ECO:0007829|PDB:4DCU" FT TURN 267..269 FT /evidence="ECO:0007829|PDB:4DCU" FT HELIX 273..284 FT /evidence="ECO:0007829|PDB:4DCU" FT STRAND 288..294 FT /evidence="ECO:0007829|PDB:4DCU" FT HELIX 296..298 FT /evidence="ECO:0007829|PDB:4DCU" FT HELIX 305..316 FT /evidence="ECO:0007829|PDB:4DCU" FT HELIX 318..320 FT /evidence="ECO:0007829|PDB:4DCU" FT STRAND 321..323 FT /evidence="ECO:0007829|PDB:5M7H" FT STRAND 325..327 FT /evidence="ECO:0007829|PDB:4DCU" FT TURN 330..332 FT /evidence="ECO:0007829|PDB:4DCU" FT HELIX 336..338 FT /evidence="ECO:0007829|PDB:4DCU" FT HELIX 339..350 FT /evidence="ECO:0007829|PDB:4DCU" FT HELIX 356..369 FT /evidence="ECO:0007829|PDB:4DCU" FT STRAND 374..377 FT /evidence="ECO:0007829|PDB:4DCV" FT STRAND 382..389 FT /evidence="ECO:0007829|PDB:4DCU" FT TURN 390..393 FT /evidence="ECO:0007829|PDB:4DCU" FT STRAND 394..400 FT /evidence="ECO:0007829|PDB:4DCU" FT HELIX 402..404 FT /evidence="ECO:0007829|PDB:4DCU" FT HELIX 407..421 FT /evidence="ECO:0007829|PDB:4DCU" FT STRAND 429..433 FT /evidence="ECO:0007829|PDB:4DCU" SQ SEQUENCE 436 AA; 48770 MW; A5CC7028FFB5A442 CRC64; MGKPVVAIVG RPNVGKSTIF NRIAGERISI VEDTPGVTRD RIYSSAEWLN YDFNLIDTGG IDIGDEPFLA QIRQQAEIAM DEADVIIFMV NGREGVTAAD EEVAKILYRT KKPVVLAVNK LDNTEMRANI YDFYSLGFGE PYPISGTHGL GLGDLLDAVA EHFKNIPETK YNEEVIQFCL IGRPNVGKSS LVNAMLGEER VIVSNVAGTT RDAVDTSFTY NQQEFVIVDT AGMRKKGKVY ETTEKYSVLR ALKAIDRSEV VAVVLDGEEG IIEQDKRIAG YAHEAGKAVV IVVNKWDAVD KDESTMKEFE ENIRDHFQFL DYAPILFMSA LTKKRIHTLM PAIIKASENH SLRVQTNVLN DVIMDAVAMN PTPTHNGSRL KIYYATQVSV KPPSFVVFVN DPELMHFSYE RFLENRIRDA FGFEGTPIKI FARARK //